Vacuolar protein sorting-associated protein 26B (VPS26B)

The protein contains 336 amino acids for an estimated molecular weight of 39155 Da.

 

Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. May be involved in retrograde transport of SORT1 but not of IGF2R. Acts redundantly with VSP26A in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1 (By similarity). (updated: April 1, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  4. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 100%
Model score: 74

(right-click above to access to more options from the contextual menu)

The reference OMIM entry for this protein is 610027

Vacuolar protein sorting 26, yeast, homolog of, b; vps26b

CLONING

Kerr et al. (2005) identified mouse Vps26b, which encodes a deduced 336-amino acid protein with a calculated molecular mass of 39.1 kD. Microarray data analysis showed that Vps26b was expressed in all mouse tissues examined. In situ hybridization of mouse embryos detected tissue- and stage-specific expression of Vps26b at all developmental stages examined. Transfected HeLa cells expressed mouse Vps26b in the cytoplasm, with low levels at the plasma membrane. Within a human lung carcinoma cell line, endogenous VPS26B and VPS26A (605506) colocalized with VPS35 (606931) in actin-rich lamellipodia at the cell surface.

GENE FUNCTION

By coprecipitation analysis using transfected human cell lines and yeast 2-hybrid analysis, Kerr et al. (2005) confirmed that mouse Vps26b interacts directly with Vps35.

GENE STRUCTURE

Kerr et al. (2005) determined that the human and mouse VPS26B genes contain 6 exons.

MAPPING

By genomic sequence analysis, Kerr et al. (2005) mapped the VPS26B gene to chromosome 11q25. They mapped the mouse Vps26b gene to chromosome 9A4. ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 610027 was added.